scholarly journals Probiotic Administration Increases Amino Acid Absorption from Plant Protein: a Placebo-Controlled, Randomized, Double-Blind, Multicenter, Crossover Study

2020 ◽  
Vol 12 (4) ◽  
pp. 1330-1339 ◽  
Author(s):  
Ralf Jäger ◽  
Javier Zaragoza ◽  
Martin Purpura ◽  
Stefania Iametti ◽  
Mauro Marengo ◽  
...  
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Amino Acid Content ◽  
Bioactive Molecules ◽  
Plant Proteins ◽  
Probiotic Supplementation ◽  
Double Blind ◽  
Pea Protein ◽  
Acid Absorption ◽  
Amino Acid Absorption

Abstract The fate of dietary protein in the gut is determined by microbial and host digestion and utilization. Fermentation of proteins generates bioactive molecules that have wide-ranging health effects on the host. The type of protein can affect amino acid absorption, with animal proteins generally being more efficiently absorbed compared with plant proteins. In contrast to animal proteins, most plant proteins, such as pea protein, are incomplete proteins. Pea protein is low in methionine and contains lower amounts of branched-chain amino acids (BCAAs), which play a crucial role in muscle health. We hypothesized that probiotic supplementation results in favorable changes in the gut microbiota, aiding the absorption of amino acids from plant proteins by the host. Fifteen physically active men (24.2 ± 5.0 years; 85.3 ± 12.9 kg; 178.0 ± 7.6 cm; 16.7 ± 5.8% body fat) co-ingested 20 g of pea protein with either AminoAlta™, a multi-strain probiotic (5 billion CFU L. paracasei LP-DG® (CNCM I-1572) plus 5 billion CFU L. paracasei LPC-S01 (DSM 26760), SOFAR S.p.A., Italy) or a placebo for 2 weeks in a randomized, double-blind, crossover design, separated by a 4-week washout period. Blood samples were taken at baseline and at 30-, 60-, 120-, and 180-min post-ingestion and analyzed for amino acid content. Probiotic administration significantly increased methionine, histidine, valine, leucine, isoleucine, tyrosine, total BCAA, and total EAA maximum concentrations (Cmax) and AUC without significantly changing the time to reach maximum concentrations. Probiotic supplementation can be an important nutritional strategy to improve post-prandial changes in blood amino acids and to overcome compositional shortcomings of plant proteins. ClinicalTrials.gov Identifier: ISRCTN38903788

Intestinal apical amino acid absorption during development of the pig

2001 ◽  
Vol 280 (1) ◽  
pp. R241-R247 ◽  
Author(s):  
Randal K. Buddington ◽  
Jan Elnif ◽  
Anna A. Puchal-Gardiner ◽  
Per T. Sangild
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Regional Differences ◽  
Apical Membrane ◽  
Saturable Absorption ◽  
Acid Absorption ◽  
Amino Acid Absorption ◽  
Apparent Diffusion ◽  
Proline Amino Acid ◽  
Small Intestines

Amino acids originating from the diet are the principal metabolic fuels for the small intestine, and although the developing intestine is exposed to dramatic changes in the types and amounts of protein, there is little known about rates of amino acid absorption across the apical membrane during development. Therefore, rates of absorption were measured for five amino acids that are substrates for the acidic (aspartate), basic (lysine), neutral (leucine and methionine), and imino (proline) amino acid carriers using intact tissues from the proximal, mid-, and distal small intestines of pigs ranging in age from 90% of gestation to 42 days after birth (12 days after weaning). Rates of absorption (sum of carrier-mediated and apparent diffusion) were highest at birth (except for proline) and declined by an average of 30% during the first 24 h of suckling. There were continuing declines for leucine, methionine, and proline but not for aspartate and lysine. Due to rapid growth of the intestine, absorption capacities for all amino acids increased faster than predicted from gains in metabolic mass. Regional differences for rates of absorption were not detected until after birth, and only for aspartate and proline. Maximum rates of saturable absorption (nmol · min−1 · mg tissue−1) by the midintestine increased during the last 10% of gestation, were highest at birth, and then declined. The contribution of apparent diffusion to amino acid absorption was lowest at birth, then increased after onset of suckling.

Dietary amino acids fed in free form or as protein do differently affect amino acid absorption in a rat everted sac model

2008 ◽  
Vol 92 (5) ◽  
pp. 529-537 ◽  
Author(s):  
J. A. Nolles ◽  
I. G. S. Peeters ◽  
B. I. Bremer ◽  
R. Moorman ◽  
R. E. Koopmanschap ◽  
...  
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Free Form ◽  
Acid Absorption ◽  
Amino Acid Absorption ◽  
Dietary Amino Acids

scholarly journals Amino acid absorption and homeostasis in mice lacking the intestinal peptide transporter PEPT1

2011 ◽  
Vol 301 (1) ◽  
pp. G128-G137 ◽  
Author(s):  
Anna-Maria Nässl ◽  
Isabel Rubio-Aliaga ◽  
Henning Fenselau ◽  
Mena Katharina Marth ◽  
Gabor Kottra ◽  
...  
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Dietary Protein ◽  
Physiological Role ◽  
Transport Processes ◽  
Peptide Transporter ◽  
Intragastric Administration ◽  
Ussing Chambers ◽  
Acid Absorption ◽  
Amino Acid Absorption

The intestinal peptide transporter PEPT1 mediates the uptake of di- and tripeptides derived from dietary protein breakdown into epithelial cells. Whereas the transporter appears to be essential to compensate for the reduced amino acid delivery in patients with mutations in amino acid transporter genes, such as in cystinuria or Hartnup disease, its physiological role in overall amino acid absorption is still not known. To assess the quantitative importance of PEPT1 in overall amino acid absorption and metabolism, PEPT1-deficient mice were studied by using brush border membrane vesicles, everted gut sacs, and Ussing chambers, as well as by transcriptome and proteome analysis of intestinal tissue samples. Neither gene expression nor proteome profiling nor functional analysis revealed evidence for any compensatory changes in the levels and/or function of transporters for free amino acids in the intestine. However, most plasma amino acid levels were increased in Pept1−/−compared with Pept1+/+animals, suggesting that amino acid handling is altered. Plasma appearance rates of15N-labeled amino acids determined after intragastric administration of a low dose of protein remained unchanged, whereas administration of a large protein load via gavage revealed marked differences in plasma appearance of selected amino acids. PEPT1 seems, therefore, important for overall amino acid absorption only after high dietary protein intake when amino acid transport processes are saturated and PEPT1 can provide additional absorption capacity. Since renal amino acid excretion remained unchanged, elevated basal concentrations of plasma amino acids in PEPT1-deficient animals seem to arise mainly from alterations in hepatic amino acid metabolism.

scholarly journals Ingestion of Free Amino Acids as Opposed to Intact Protein Increases Amino Acid Absorption but Does Not Further Augment Postprandial Muscle Protein Synthesis Rates

2020 ◽  
Vol 4 (Supplement_2) ◽  
pp. 673-673
Author(s):  
Michelle E G Weijzen ◽  
Rob JJ van Gassel ◽  
Imre W K Kouw ◽  
Stefan H M Gorissen ◽  
Marcel CG van de Poll ◽  
...  
Keyword(s):  
Amino Acids ◽  
Protein Synthesis ◽  
Amino Acid ◽  
Free Amino Acids ◽  
Free Amino ◽  
Muscle Protein ◽  
Muscle Protein Synthesis ◽  
Protein Digestion ◽  
Acid Absorption ◽  
Amino Acid Absorption

Abstract Objectives The rate of protein digestion and amino acid absorption determines the postprandial rise in circulating amino acids and, as such, modulates postprandial muscle protein synthesis rates. This study compares protein digestion and amino acid absorption kinetics and the subsequent muscle protein synthetic response following ingestion of intact protein versus an equivalent amount of free, crystalline amino acids. Methods Twenty-four healthy, young subjects (age: 22 ± 3 y, BMI: 23 ± 2 kg·m−2, sex: 12 M/12F) ingested 30 g intrinsically L-[1–13C]-phenylalanine and L-[1–13C]-leucine labeled milk protein (PROT; n = 12) or an equivalent amount of free amino acids (AA; n = 12). In addition, subjects received primed continuous L-[ring-2H5]-phenylalanine, L-[ring-3,5–2H2]-tyrosine, and L-[1–13C]-leucine infusions. Blood samples and muscle biopsies were obtained frequently to assess protein digestion and amino acid absorption kinetics and subsequent muscle protein synthesis rates over a 6 h postprandial period. An unpaired t-test was used to compare overall exogenous phenylalanine release in plasma. For other parameters repeated measures ANOVA were applied to determine differences between groups over time (time as within, and group as between-subjects factor). Data are expressed as mean ± SD. Results Postprandial plasma amino acid concentrations and exogenous phenylalanine appearance rates increased after ingestion of PROT and AA (both, P < 0.001), with a greater increase following ingestion of AA when compared to PROT (time*group interaction P < 0.001). Exogenous phenylalanine release in plasma assessed over the 6 h postprandial period, was greater in AA (76 ± 9%) compared with PROT (59 ± 10%; P < 0.001). Ingestion of AA and PROT strongly increased muscle protein synthesis rates based upon L-[ring-2H5]-phenylalanine (time effect P < 0.001), with no differences between groups (from 0.037 ± 0.015 to 0.053 ± 0.014%·h−1 and from 0.039 ± 0.016 to 0.051 ± 0.010%·h−1, respectively; time*group interaction P = 0.629). Conclusions Ingestion of free amino acids as opposed to intact milk protein is followed by more rapid amino acid absorption and greater postprandial plasma amino acid availability, but this does not further augment postprandial muscle protein synthesis rates. Funding Sources This research did not receive external funding.

scholarly journals Amino Acid Absorption in the Locust (Schistocerca Gregaria Forsk.)

1959 ◽  
Vol 36 (3) ◽  
pp. 533-545
Author(s):  
J. E. TREHERNE
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Chromatographic Analysis ◽  
Schistocerca Gregaria ◽  
Rapid Decrease ◽  
Acid Absorption ◽  
Rapid Movement ◽  
Amino Acid Absorption ◽  
Rapid Exchange ◽  
High Concentrations

1. Chromatographic analysis of the haemolymph revealed the presence of ten amino acids of which glycine and serine occurred in the relatively high concentrations of 33.2 and 34.6 mM./l. respectively. These two amino acids, together with glutamine (10.9 mM./l), were selected for the study of absorption from the gutlumen. 2. An experimental solution containing 14C-labelled glycine and serine was injected into the gut lumen and the subsequent changes in concentration and radioactivity of the gut fluid were followed. 3. The uptake of 14C-labelled glycine and serine was shown to occur rapidly in the mid-gut region and especially from the lumen of the caeca. 4. The concentrations of glycine and serine, and also of glutamine, in the caecal fluid were found to increase significantly above their concentrations in the haemolymph, an effect which was paralleled by a relatively rapid decrease in fluid volume. During this time rapid exchange of 14C-labelled glycine and serine between the haemolymph and the gut lumen was demonstrated. 5. On the basis of these observations it was concluded that the net absorption of these substances depended, in part at least, upon the diffusion gradient created by the relatively rapid movement of water into the haemolymph.

scholarly journals Optimising amino acid absorption: essential to improve nitrogen balance and metabolic control in phenylketonuria

2018 ◽  
Vol 32 (1) ◽  
pp. 70-78 ◽  
Author(s):  
Anita MacDonald ◽  
Rani H. Singh ◽  
Júlio César Rocha ◽  
Francjan J. van Spronsen
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Free Amino ◽  
N Balance ◽  
Intact Protein ◽  
Hydroxylase Deficiency ◽  
Strict Adherence ◽  
Acid Absorption ◽  
Amino Acid Absorption ◽  
The Impact

AbstractIt has been nearly 70 years since the discovery that strict adherence to a diet low in phenylalanine prevents severe neurological sequelae in patients with phenylalanine hydroxylase deficiency (phenylketonuria; PKU). Today, dietary treatment with restricted phenylalanine intake supplemented with non-phenylalanine amino acids to support growth and maintain a healthy body composition remains the mainstay of therapy. However, a better understanding is needed of the factors that influence N balance in the context of amino acid supplementation. The aim of the present paper is to summarise considerations for improving N balance in patients with PKU, with a focus on gaining greater understanding of amino acid absorption, disposition and utilisation. In addition, the impact of phenylalanine-free amino acids on 24 h blood phenylalanine/tyrosine circadian rhythm is evaluated. We compare the effects of administering intact protein v. free amino acid on protein metabolism and discuss the possibility of improving outcomes by administering amino acid mixtures so that their absorption profile mimics that of intact protein. Protein substitutes with the ability to delay absorption of phenylalanine and tyrosine, mimicking physiological absorption kinetics, are expected to improve the rate of assimilation into protein and minimise fluctuations in quantitative plasma amino acid levels. They may also help maintain normal glycaemia and satiety sensation. This is likely to play an important role in improving the management of patients with PKU.

scholarly journals The role of glutathione in amino-acid absorption. Lack of correlation between glutathione turnover and amino-acid absorption by the yeast Candida utilis

1981 ◽  
Vol 194 (1) ◽  
pp. 63-70 ◽  
Author(s):  
R J Robins ◽  
D D Davies
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Half Life ◽  
Candida Utilis ◽  
Free Medium ◽  
Gamma Glutamyl ◽  
Acid Absorption ◽  
Amino Acid Absorption

The rate of degradation of glutathione has been determined in the yeast Candida utilis by using a method that minimizes the effect of amino-acid recycling. When yeast are grown in amino-acid-free medium, the half-life of glutathione was found to be 230 min. C. utilis was also found to absorb various L-amino acids rapidly without producing any significant decrease in the half-life of glutathione. While the gamma-glutamyl cycle is thus operating in C. utilis, the rate of degradation of glutathione is found to be 100 times too slow for the cycle to be mediating the transport of these amino acids.

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